Efficient expression in E. coli of an enantioselective nitrile hydratase from Rhodococcus erythropolis

Song, Liya and Yuan, Hong Jie and Coffey, Lee and Doran, John and Wang, Mei Xiang and Qian, Shijun and O'Reilly, Catherine (2008) Efficient expression in E. coli of an enantioselective nitrile hydratase from Rhodococcus erythropolis. Biotechnology Letters, 30 (4). pp. 755-762. ISSN 0141-5492

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Abstract

The genes encoding an enantioselective nitrile hydratase (NHase) from Rhodococcus erythropolis AJ270 have been cloned and an active NHase has been produced in Escherichia coli. Maximal activity was found when the genes encoding the α- and β-subunits were transcribed as one unit and the gene encoding the P44k activator protein as a separate ORF on a single replicon. Addition of n-butyric acid and FeSO4 could improve NHase activity. Coexpression of the GroEL-GroES chaperone proteins increased activity in the absence of P44k protein but had no effect in the presence of P44k. The recombinant enzyme was highly enantioselective in the synthesis of S-(+)-3-benzoyloxy- 4-cyanobutyramide from the prochiral substrate 3-benzoyloxyglutaronitrile.

Item Type:	Article
Additional Information:	Funding Information: Acknowledgements This work was funded by the China-Ireland Collaboration Fund through Science Foundation Ireland and the Ministry of Science and Technology, China and by an EMBARK Ph.D. studentship to Lee Coffey.
Uncontrolled Keywords:	/dk/atira/pure/subjectarea/asjc/1300/1305
Departments or Groups:
Depositing User:	Admin SSL
Date Deposited:	19 Oct 2022 23:04
Last Modified:	23 Jun 2023 19:40
URI:	http://repository-testing.wit.ie/id/eprint/3935

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